Article
Trithorax requires Hsp90 for maintenance of active chromatin at sites of gene expression.
Proceedings of the National Academy of Sciences of the United States of America - 27 Jan 2009
Tariq Muhammad, Nussbaumer Ute, Chen Yujie, Beisel Christian, Paro Renato
Abstract excerpt
Molecular chaperone heat-shock protein 90 kDa (Hsp90) is known to facilitate the conformational maturation of a diverse range of proteins involved in different signal transduction pathways during development. Recent studies have implicated Hsp90 in transcriptional regulation and an important role for Hsp90 in epigenetic processes has been proposed. Importantly, genetic and pharmacological perturbation of Hsp90...
Topics
- Animals
- Cell Line
- Chromatin
- Chromosomal Proteins, Non-Histone
- Drosophila Proteins
- Drosophila melanogaster
- Gene Expression Regulation
- Genes, Insect
- HSP90 Heat-Shock Proteins
- Mutation